RT Journal Article SR Electronic(1) A1 Gillet, Laurent A1 May, Janet S. A1 Stevenson, Philip G.YR 2009 T1 In vivo importance of heparan sulfate-binding glycoproteins for murid herpesvirus-4 infection JF Journal of General Virology, VO 90 IS 3 SP 602 OP 613 DO https://doi.org/10.1099/vir.0.005785-0 PB Microbiology Society, SN 1465-2099, AB Many herpesviruses bind to heparan sulfate (HS). Murid herpesvirus-4 (MuHV-4) does so via its envelope glycoproteins gp70 and gH/gL. MuHV-4 gp150 further regulates an HS-independent interaction to make that HS-dependent too. Cell binding by MuHV-4 virions is consequently strongly HS-dependent. Gp70 and gH/gL show some in vitro redundancy: an antibody-mediated blockade of HS binding by one is well tolerated, whereas a blockade of both severely impairs infection. In order to understand the importance of HS binding for MuHV-4 in vivo, we generated mutants lacking both gL and gp70. As expected, gL−gp70− MuHV-4 showed very poor cell binding. It infected mice at high dose but not at low dose, indicating defective host entry. But once entry occurred, host colonization, which for MuHV-4 is relatively independent of the infection dose, was remarkably normal. The gL−gp70− entry deficit was much greater than that of gL− or gp70− single knockouts. And gp150 disruption, which allows HS-independent cell binding, largely rescued the gL−gp70− cell binding and host entry deficits. Thus, it appeared that MuHV-4 HS binding is important in vivo, principally for efficient host entry., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.005785-0